Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

47.0K
Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
47.0K
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

5.3K
5.3K
Globular Proteins01:27

Globular Proteins

10.0K
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
10.0K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

5.9K
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
5.9K
Protein Folding01:22

Protein Folding

127.3K
Overview
127.3K
Protein Organization01:13

Protein Organization

157.6K
Overview
157.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The master molecule that built biology: How water shaped the chemistry of life.

Protein science : a publication of the Protein Society·2026
Same author

50 years in the shadow of the Ramachandran plot.

Protein science : a publication of the Protein Society·2025
Same author

From propensities to patterns to principles in protein folding.

Proteins·2023
Same author

Opinion: Protein folds vs. protein folding: Differing questions, different challenges.

Proceedings of the National Academy of Sciences of the United States of America·2022
Same author

Reframing the Protein Folding Problem: Entropy as Organizer.

Biochemistry·2021
Same author

Protein folding - seeing is deceiving.

Protein science : a publication of the Protein Society·2021

Related Experiment Video

Updated: Jan 30, 2026

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins
11:30

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins

Published on: August 31, 2019

25.2K

Ramachandran maps for side chains in globular proteins.

George D Rose1

  • 1T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.

Proteins
|January 11, 2019
PubMed
Summary
This summary is machine-generated.

Side chain conformations in proteins are influenced by steric repulsion, similar to backbone angles. This conformational bias is inherent at the covalent level, impacting protein folding and secondary structure.

Keywords:
Ramachandran mapsprotein foldingresidue side chainssteric restrictions

More Related Videos

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

813
Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

2.0K

Related Experiment Videos

Last Updated: Jan 30, 2026

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins
11:30

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins

Published on: August 31, 2019

25.2K
Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

813
Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

2.0K

Area of Science:

  • Protein structure and conformational analysis
  • Computational biology and bioinformatics

Background:

  • The Ramachandran plot for backbone angles (ϕ,ψ) is crucial for protein structure analysis.
  • Side chain conformational preferences (χ-angles) have been less explored compared to backbone angles.
  • Existing research often relies on side chain libraries extracted from known protein structures.

Purpose of the Study:

  • To analyze side chain conformational preferences using backbone-based maps in blocked monopeptides.
  • To investigate the role of steric repulsion in determining side chain biases.
  • To compare side chain biases in monopeptides with those observed in high-resolution protein structures.

Main Methods:

  • Generation of backbone-based maps for side chains in blocked monopeptides.
  • Analysis based solely on hard-sphere steric repulsion.
  • Comparison of derived side chain biases with existing data from protein structures.

Main Results:

  • Side chain biases in monopeptides show remarkable similarities to those in high-resolution protein structures.
  • Conformational bias for side chains is established at the covalent level, pre-folding.
  • Side chains experience fewer steric restrictions in backbone conformations corresponding to α-helices and β-sheets (α/β basins).

Conclusions:

  • Steric repulsion alone favors α/β basins for monopeptides, mirroring preferences in repetitive secondary structures.
  • This inherent conformational bias contributes to the entropic cost of side chain localization in proteins.
  • There is an energetically unfrustrated compatibility between monopeptide conformational preferences and repetitive protein secondary structures.